CYT1_HORVU
ID CYT1_HORVU Reviewed; 107 AA.
AC Q9LEI7; Q4W4C8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Cysteine proteinase inhibitor;
DE AltName: Full=Cystatin;
DE AltName: Full=Hv-CPI;
GN Name=ICY; Synonyms=CPI;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Bomi; TISSUE=Endosperm;
RX PubMed=11414618; DOI=10.1023/a:1010697204686;
RA Gaddour K., Vicente-Carbajosa J., Lara P., Isabel-Lamoneda I., Diaz I.,
RA Carbonero P.;
RT "A constitutive cystatin-encoding gene from barley (Icy) responds
RT differentially to abiotic stimuli.";
RL Plant Mol. Biol. 45:599-608(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY GIBBERELLIC ACID, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Igri;
RX PubMed=15611149; DOI=10.1093/jxb/eri033;
RA Martinez M., Rubio-Somoza I., Fuentes R., Lara P., Carbonero P., Diaz I.;
RT "The barley cystatin gene (Icy) is regulated by DOF transcription factors
RT in aleurone cells upon germination.";
RL J. Exp. Bot. 56:547-556(2005).
RN [3]
RP MUTAGENESIS OF ARG-38; GLN-63; CYS-68 AND LYS-92, AND FUNCTION.
RX PubMed=14558689; DOI=10.1094/mpmi.2003.16.10.876;
RA Martinez M., Lopez-Solanilla E., Rodriguez-Palenzuela P., Carbonero P.,
RA Diaz I.;
RT "Inhibition of plant-pathogenic fungi by the barley cystatin Hv-CPI (gene
RT Icy) is not associated with its cysteine-proteinase inhibitory
RT properties.";
RL Mol. Plant Microbe Interact. 16:876-883(2003).
RN [4]
RP INDUCTION BY GIBBERELLIC ACID; ABSCISIC ACID; GERMINATION.
RX PubMed=12598566; DOI=10.1093/jxb/erg099;
RA Martinez M., Rubio-Somoza I., Carbonero P., Diaz I.;
RT "A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB)
RT induced by GA in aleurone cells is under circadian control in leaves.";
RL J. Exp. Bot. 54:951-959(2003).
CC -!- FUNCTION: Inhibits papain, ficin, cathepsin B and, to a lesser extent,
CC chymopapain, but is inactive against bromelain. Inhibits the growth of
CC pathogenic fungi. Regulated by the DOF transcription factors SAD
CC (activator) and BPBF (repressor). {ECO:0000269|PubMed:11414618,
CC ECO:0000269|PubMed:14558689}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos, developing endosperms,
CC leaves, roots, flowers and pollen grains. {ECO:0000269|PubMed:11414618,
CC ECO:0000269|PubMed:15611149}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed germination.
CC {ECO:0000269|PubMed:15611149}.
CC -!- INDUCTION: Up-regulated by dark and cold shock, anaerobiosis and upon
CC seed imbibition. Repressed by gibberellic acid treatment in aleurones,
CC but not in leaves. Not affected by abscisic acid treatment.
CC {ECO:0000269|PubMed:11414618, ECO:0000269|PubMed:12598566,
CC ECO:0000269|PubMed:15611149}.
CC -!- SIMILARITY: Belongs to the cystatin family. Phytocystatin subfamily.
CC {ECO:0000305}.
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DR EMBL; Y12068; CAA72790.1; -; mRNA.
DR EMBL; AJ536590; CAD60537.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LEI7; -.
DR SMR; Q9LEI7; -.
DR MEROPS; I25.051; -.
DR ExpressionAtlas; Q9LEI7; baseline.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR027214; Cystatin.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR018073; Prot_inh_cystat_CS.
DR PANTHER; PTHR11413; PTHR11413; 1.
DR Pfam; PF16845; SQAPI; 1.
DR SMART; SM00043; CY; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
DR PROSITE; PS00287; CYSTATIN; 1.
PE 1: Evidence at protein level;
KW Plant defense; Protease inhibitor; Thiol protease inhibitor.
FT CHAIN 1..107
FT /note="Cysteine proteinase inhibitor"
FT /id="PRO_0000312803"
FT DOMAIN 18..107
FT /note="Cystatin"
FT MOTIF 63..67
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT SITE 18
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT MUTAGEN 38
FT /note="R->G: Decreased cystatin activity, but no effect on
FT anti-fungal activity."
FT /evidence="ECO:0000269|PubMed:14558689"
FT MUTAGEN 63
FT /note="Q->L,P: Decreased cystatin activity, but no effect
FT on anti-fungal activity."
FT /evidence="ECO:0000269|PubMed:14558689"
FT MUTAGEN 68
FT /note="C->G: Increased cystatin activity."
FT /evidence="ECO:0000269|PubMed:14558689"
FT MUTAGEN 92
FT /note="K->P: Loss of anti-fungal activity, but retains some
FT cystatin activity."
FT /evidence="ECO:0000269|PubMed:14558689"
FT CONFLICT 6
FT /note="H -> Q (in Ref. 2; CAD60537)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="K -> R (in Ref. 2; CAD60537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 107 AA; 11781 MW; 8C185786AE13623A CRC64;
MAEAAHGGGL RGRGVLLGGV QDAPAGREND LETIELARFA VAEHNAKANA LLEFEKLVKV
RQQVVAGCMH YFTIEVKEGG AKKLYEAKVW EKAWENFKQL QEFKPAA
